1jw0

From Proteopedia

(Difference between revisions)

Revision as of 07:14, 11 October 2017

Structure of cephalosporin acylase in complex with glutarate

Structural highlights

1jw0 is a 2 chain structure with sequence from Aj 2067. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1jvz
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[G7AC_BREDI] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Can not efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is obtained by environmentally toxic chemical deacylation of cephalosporin C (CPC). Thus, the enzymatic conversion of CPC to 7-ACA by cephalosporin acylase (CA) would be of great interest. However, CAs use glutaryl-7-ACA (GL-7-ACA) as a primary substrate and the enzyme has low turnover rates for CPC. RESULTS: The binary complex structures of CA with GL-7-ACA and glutarate (the side-chain of GL-7-ACA) show extensive interactions between the glutaryl moiety of GL-7-ACA and the seven residues that form the side-chain pocket. These interactions explain why the D-alpha-aminoadipyl side-chain of CPC yields a poorer substrate than GL-7-ACA. CONCLUSIONS: This understanding of the nature of substrate specificity may be useful in the design of an enzyme with an improved performance for the conversion of CPC to 7-ACA. Additionally, the catalytic mechanism of the deacylation reaction was revealed by the ligand bound structures.

Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity.,Kim Y, Hol WG Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kim Y, Yoon K, Khang Y, Turley S, Hol WG. The 2.0 A crystal structure of cephalosporin acylase. Structure. 2000 Oct 15;8(10):1059-68. PMID:11080627
↑ Kim Y, Hol WG. Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity. Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jw0"

@@ Line 1: / Line 1: @@
 ==Structure of cephalosporin acylase in complex with glutarate==
 <StructureSection load='1jw0' size='340' side='right' caption='[[1jw0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jvz|1jvz]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jw0 OCA], [http://pdbe.org/1jw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1jw0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jw0 OCA], [http://pdbe.org/1jw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1jw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jw0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jw0 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1jw0" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cephalosporin acylase|Cephalosporin acylase]]
 == References ==
 <references/>

1jw0

From Proteopedia

Revision as of 07:14, 11 October 2017

Structure of cephalosporin acylase in complex with glutarate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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